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SIGM1_REOVL
ID   SIGM1_REOVL             Reviewed;         470 AA.
AC   P04506; A4ZY30; P07937;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   02-JUN-2021, entry version 113.
DE   RecName: Full=Outer capsid protein sigma-1;
DE            Short=Sigma1;
DE   AltName: Full=Cell attachment protein;
DE   AltName: Full=Hemagglutinin;
GN   Name=S1;
OS   Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Orthoreovirus.
OX   NCBI_TaxID=10884;
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3855545; DOI=10.1073/pnas.82.1.24;
RA   Cashdollar L.W., Chmelo R.A., Wiener J.R., Joklik W.K.;
RT   "Sequences of the S1 genes of the three serotypes of reovirus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:24-28(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2430568; DOI=10.1016/0006-291x(86)90761-8;
RA   Munemitsu S.M., Atwater J.A., Samuel C.E.;
RT   "Biosynthesis of reovirus-specified polypeptides. Molecular cDNA cloning
RT   and nucleotide sequence of the reovirus serotype 1 Lang strain bicistronic
RT   s1 mRNA which encodes the minor capsid polypeptide sigma 1a and the
RT   nonstructural polypeptide sigma 1bNS.";
RL   Biochem. Biophys. Res. Commun. 140:508-514(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2305549; DOI=10.1016/0042-6822(90)90093-7;
RA   Duncan R., Horne D., Cashdollar L.W., Joklik W.K., Lee P.W.K.;
RT   "Identification of conserved domains in the cell attachment proteins of the
RT   three serotypes of reovirus.";
RL   Virology 174:399-409(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2335823; DOI=10.1128/jvi.64.6.2976-2989.1990;
RA   Nibert M.L., Dermody T.S., Fields B.N.;
RT   "Structure of the reovirus cell-attachment protein: a model for the domain
RT   organization of sigma 1.";
RL   J. Virol. 64:2976-2989(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Infectious clone;
RX   PubMed=18005692; DOI=10.1016/j.chom.2007.03.003;
RA   Kobayashi T., Antar A.A., Boehme K.W., Danthi P., Eby E.A., Guglielmi K.M.,
RA   Holm G.H., Johnson E.M., Maginnis M.S., Naik S., Skelton W.B., Wetzel J.D.,
RA   Wilson G.J., Chappell J.D., Dermody T.S.;
RT   "A plasmid-based reverse genetics system for animal double-stranded RNA
RT   viruses.";
RL   Cell Host Microbe 1:147-157(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-21.
RX   PubMed=6158163; DOI=10.1016/0042-6822(80)90154-3;
RA   Li J.K.-K., Keene J.D., Scheible P.P., Joklik W.K.;
RT   "Nature of the 3'-terminal sequences of the plus and minus strands of the
RT   S1 gene of reovirus serotypes 1, 2 and 3.";
RL   Virology 105:41-51(1980).
CC   -!- FUNCTION: Fiber-like molecule that attaches the virion to the host cell
CC       membrane by binding to the primary receptor F11R/JAM-A and to sialic
CC       acid containing proteins (coreceptor). The interaction of sigma-1 with
CC       F11R is required for NF-kB activation and apoptosis. Binding to both
CC       sialic acid and F11R is required to induce maximal levels of apoptosis
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. Interacts (via the head region) with human F11R
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Found in the outer
CC       capsid (36 copies). {ECO:0000250}.
CC   -!- PTM: Undergoes dramatic conformational rearrangements during viral
CC       disassembly in the endocytic pathway. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the orthoreovirus sigma-1 protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA47276.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA66877.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M10260; AAA66877.1; ALT_FRAME; Genomic_RNA.
DR   EMBL; M14779; AAA47276.1; ALT_FRAME; Genomic_RNA.
DR   EMBL; M32860; AAA47267.1; -; Genomic_RNA.
DR   EMBL; M35963; AAA47242.1; -; Genomic_RNA.
DR   EMBL; EF494445; ABP48923.1; -; Genomic_RNA.
DR   EMBL; AH002406; AAA47240.1; -; Genomic_RNA.
DR   PIR; A04122; HMXRH1.
DR   PIR; A34829; HMXRL1.
DR   PDB; 4GU3; X-ray; 3.60 A; A/B/C=261-470.
DR   PDB; 4GU4; X-ray; 3.50 A; A/B/C=261-470.
DR   PDB; 4ODB; X-ray; 3.20 A; A/B/C=308-470.
DR   PDB; 4XC5; X-ray; 2.20 A; A/B/C=308-470.
DR   PDB; 5MHS; X-ray; 3.70 A; A/B/C=308-470.
DR   PDB; 6GAJ; X-ray; 1.35 A; A/B/C=29-159.
DR   PDB; 6GAK; X-ray; 1.43 A; A/B/C=29-159.
DR   PDB; 6GAO; X-ray; 2.10 A; A/B/C=29-264.
DR   PDBsum; 4GU3; -.
DR   PDBsum; 4GU4; -.
DR   PDBsum; 4ODB; -.
DR   PDBsum; 4XC5; -.
DR   PDBsum; 5MHS; -.
DR   PDBsum; 6GAJ; -.
DR   PDBsum; 6GAK; -.
DR   PDBsum; 6GAO; -.
DR   SMR; P04506; -.
DR   ABCD; P04506; 1 sequenced antibody.
DR   Proteomes; UP000007253; Genome.
DR   GO; GO:0019028; C:viral capsid; IDA:CACAO.
DR   GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR008982; Adenovirus_pIV-like_att.
DR   InterPro; IPR002592; Vir_attach_sigma1_reovir.
DR   Pfam; PF01664; Reo_sigma1; 1.
DR   SUPFAM; SSF49835; SSF49835; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Coiled coil; Glycoprotein; Hemagglutinin;
KW   Host-virus interaction; Outer capsid protein; Reference proteome;
KW   Viral attachment to host cell; Virion; Virus entry into host cell.
FT   CHAIN           1..470
FT                   /note="Outer capsid protein sigma-1"
FT                   /id="PRO_0000040667"
FT   REGION          1..324
FT                   /note="Tail"
FT   REGION          325..470
FT                   /note="Head"
FT   COILED          26..46
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        91
FT                   /note="V -> G (in Ref. 1; AAA66877 and 2; AAA47276)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="S -> F (in Ref. 1; AAA66877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384
FT                   /note="V -> L (in Ref. 2; AAA47276)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="L -> W (in Ref. 4; AAA47242)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..156
FT                   /evidence="ECO:0007829|PDB:6GAJ"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   STRAND          193..196
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   HELIX           215..217
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   STRAND          219..224
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   TURN            234..236
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:6GAO"
FT   STRAND          274..278
FT                   /evidence="ECO:0007829|PDB:4GU4"
FT   STRAND          281..285
FT                   /evidence="ECO:0007829|PDB:4GU4"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:4GU4"
FT   STRAND          293..296
FT                   /evidence="ECO:0007829|PDB:4GU4"
FT   STRAND          299..304
FT                   /evidence="ECO:0007829|PDB:4GU4"
FT   STRAND          315..318
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   TURN            319..322
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          323..326
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   HELIX           328..331
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          333..345
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          348..361
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          364..369
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          372..375
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          379..386
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   TURN            387..390
FT                   /evidence="ECO:0007829|PDB:4ODB"
FT   HELIX           397..400
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          409..420
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          423..437
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          440..449
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          454..458
FT                   /evidence="ECO:0007829|PDB:4XC5"
FT   STRAND          461..466
FT                   /evidence="ECO:0007829|PDB:4XC5"
SQ   SEQUENCE   470 AA;  51404 MW;  F4D18989AD54491C CRC64;
     MDASLITEIR KIVLQLSVSS NGSQSKEIEE IKKQVQVNVD DIRAANIKLD GLGRQIADIS
     NSISTIESRL GEMDNRLVGI SSQVTQLSNS VSQNTQSISS LGDRINAVEP RVDSLDTVTS
     NLTGRTSTLE ADVGSLRTEL AALTTRVTTE VTRLDGLINS GQNSIGELST RLSNVETSMV
     TTAGRGLQKN GNTLNVIVGN GMWFNSSNQL QLDLSGQSKG VGFVGTGMVV KIDTNYFAYN
     SNGEITLVSQ INELPSRVST LESAKIDSVL PPLTVREASG VRTLSFGYDT SDFTIINSVL
     SLRSRLTLPT YRYPLELDTA NNRVQVADRF GMRTGTWTGQ LQYQHPQLSW RANVTLNLMK
     VDDWLVLSFS QMTTNSIMAD GKFVINFVSG LSSGWQTGDT EPSSTIDPLS TTFAAVQFLN
     NGQRIDAFRI MGVSEWTDGE LEIKNYGGTY TGHTQVYWAP WTIMYPCNVR
 
 
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